Slow conformational exchange and overall rocking motion in ubiquitin protein crystals

X-ray crystallography is the main method for protein structure determination. Here the authors combine solid-state NMR measurements and molecular dynamics simulations and show that crystal packing alters the thermodynamics and kinetics of local conformational exchange as well as overall rocking moti...

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Autores principales:	Vilius Kurauskas, Sergei A. Izmailov, Olga N. Rogacheva, Audrey Hessel, Isabel Ayala, Joyce Woodhouse, Anastasya Shilova, Yi Xue, Tairan Yuwen, Nicolas Coquelle, Jacques-Philippe Colletier, Nikolai R. Skrynnikov, Paul Schanda
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/78a4400245f74b8a820610acebc867aa
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spelling	oai:doaj.org-article:78a4400245f74b8a820610acebc867aa2021-12-02T10:48:28ZSlow conformational exchange and overall rocking motion in ubiquitin protein crystals10.1038/s41467-017-00165-82041-1723https://doaj.org/article/78a4400245f74b8a820610acebc867aa2017-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-00165-8https://doaj.org/toc/2041-1723X-ray crystallography is the main method for protein structure determination. Here the authors combine solid-state NMR measurements and molecular dynamics simulations and show that crystal packing alters the thermodynamics and kinetics of local conformational exchange as well as overall rocking motion of protein molecules in the crystal lattice.Vilius KurauskasSergei A. IzmailovOlga N. RogachevaAudrey HesselIsabel AyalaJoyce WoodhouseAnastasya ShilovaYi XueTairan YuwenNicolas CoquelleJacques-Philippe ColletierNikolai R. SkrynnikovPaul SchandaNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Vilius Kurauskas Sergei A. Izmailov Olga N. Rogacheva Audrey Hessel Isabel Ayala Joyce Woodhouse Anastasya Shilova Yi Xue Tairan Yuwen Nicolas Coquelle Jacques-Philippe Colletier Nikolai R. Skrynnikov Paul Schanda Slow conformational exchange and overall rocking motion in ubiquitin protein crystals
description	X-ray crystallography is the main method for protein structure determination. Here the authors combine solid-state NMR measurements and molecular dynamics simulations and show that crystal packing alters the thermodynamics and kinetics of local conformational exchange as well as overall rocking motion of protein molecules in the crystal lattice.
format	article
author	Vilius Kurauskas Sergei A. Izmailov Olga N. Rogacheva Audrey Hessel Isabel Ayala Joyce Woodhouse Anastasya Shilova Yi Xue Tairan Yuwen Nicolas Coquelle Jacques-Philippe Colletier Nikolai R. Skrynnikov Paul Schanda
author_facet	Vilius Kurauskas Sergei A. Izmailov Olga N. Rogacheva Audrey Hessel Isabel Ayala Joyce Woodhouse Anastasya Shilova Yi Xue Tairan Yuwen Nicolas Coquelle Jacques-Philippe Colletier Nikolai R. Skrynnikov Paul Schanda
author_sort	Vilius Kurauskas
title	Slow conformational exchange and overall rocking motion in ubiquitin protein crystals
title_short	Slow conformational exchange and overall rocking motion in ubiquitin protein crystals
title_full	Slow conformational exchange and overall rocking motion in ubiquitin protein crystals
title_fullStr	Slow conformational exchange and overall rocking motion in ubiquitin protein crystals
title_full_unstemmed	Slow conformational exchange and overall rocking motion in ubiquitin protein crystals
title_sort	slow conformational exchange and overall rocking motion in ubiquitin protein crystals
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/78a4400245f74b8a820610acebc867aa
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Slow conformational exchange and overall rocking motion in ubiquitin protein crystals

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